APOA1_HUMAN
ID APOA1_HUMAN Reviewed; 267 AA.
AC P02647; A8K866; Q6LDN9; Q6Q785; Q9UCS8; Q9UCT8;
DT 21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT 21-JUL-1986, sequence version 1.
DT 03-AUG-2022, entry version 261.
DE RecName: Full=Apolipoprotein A-I {ECO:0000305};
DE Short=Apo-AI;
DE Short=ApoA-I;
DE AltName: Full=Apolipoprotein A1;
DE Contains:
DE RecName: Full=Proapolipoprotein A-I;
DE Short=ProapoA-I;
DE Contains:
DE RecName: Full=Truncated apolipoprotein A-I;
DE AltName: Full=Apolipoprotein A-I(1-242);
DE Flags: Precursor;
GN Name=APOA1 {ECO:0000312|HGNC:HGNC:600};
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=6406984; DOI=10.1093/nar/11.9.2827;
RA Shoulders C.C., Kornblihtt A.R., Munro B.S., Baralle F.E.;
RT "Gene structure of human apolipoprotein A1.";
RL Nucleic Acids Res. 11:2827-2837(1983).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=6304641; DOI=10.1093/nar/11.11.3703;
RA Cheung P., Chan L.;
RT "Nucleotide sequence of cloned cDNA of human apolipoprotein A-I.";
RL Nucleic Acids Res. 11:3703-3715(1983).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=6413973; DOI=10.1073/pnas.80.20.6147;
RA Karathanasis S.K., Zannis V.I., Breslow J.L.;
RT "Isolation and characterization of the human apolipoprotein A-I gene.";
RL Proc. Natl. Acad. Sci. U.S.A. 80:6147-6151(1983).
RN [4]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=6207999; DOI=10.1089/dna.1.1984.3.309;
RA Seilhamer J.J., Protter A.A., Frossard P., Levy-Wilson B.;
RT "Isolation and DNA sequence of full-length cDNA and of the entire gene for
RT human apolipoprotein AI -- discovery of a new genetic polymorphism in the
RT apo AI gene.";
RL DNA 3:309-317(1984).
RN [5]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=6328445; DOI=10.1093/nar/12.9.3917;
RA Sharpe C.R., Sidoli A., Shelley C.S., Lucero M.A., Shoulders C.C.,
RA Baralle F.E.;
RT "Human apolipoproteins AI, AII, CII and CIII. cDNA sequences and mRNA
RT abundance.";
RL Nucleic Acids Res. 12:3917-3932(1984).
RN [6]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=6198645; DOI=10.1073/pnas.81.1.66;
RA Law S.W., Brewer H.B. Jr.;
RT "Nucleotide sequence and the encoded amino acids of human apolipoprotein A-
RT I mRNA.";
RL Proc. Natl. Acad. Sci. U.S.A. 81:66-70(1984).
RN [7]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=2995392; DOI=10.1016/s0021-9258(17)38949-4;
RA Law S.W., Brewer H.B. Jr.;
RT "Tangier disease. The complete mRNA sequence encoding for preproapo-A-I.";
RL J. Biol. Chem. 260:12810-12814(1985).
RN [8]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] (VARIANT TANGIER).
RX PubMed=3129297; DOI=10.1111/j.1432-1033.1988.tb14022.x;
RA Makrides S.C., Ruiz-Opazo N., Hayden M.R., Nussbaum A.L., Breslow J.L.,
RA Zannis V.I.;
RT "Sequence and expression of Tangier apoA-I gene.";
RL Eur. J. Biochem. 173:465-471(1988).
RN [9]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=2673706; DOI=10.1089/dna.1.1989.8.429;
RA Moguilevsky N., Roobol C., Loriau R., Guillaume J.P., Jacobs P.,
RA Cravador A., Herzog A., Brouwers L., Scarso A., Gilles P., Holmquist L.,
RA Carlson L.A., Bollen A.;
RT "Production of human recombinant proapolipoprotein A-I in Escherichia coli:
RT purification and biochemical characterization.";
RL DNA 8:429-436(1989).
RN [10]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND VARIANT THR-61.
RX PubMed=15108119; DOI=10.1007/s00439-004-1106-x;
RA Fullerton S.M., Buchanan A.V., Sonpar V.A., Taylor S.L., Smith J.D.,
RA Carlson C.S., Salomaa V., Stengaard J.H., Boerwinkle E., Clark A.G.,
RA Nickerson D.A., Weiss K.M.;
RT "The effects of scale: variation in the APOA1/C3/A4/A5 gene cluster.";
RL Hum. Genet. 115:36-56(2004).
RN [11]
RP NUCLEOTIDE SEQUENCE [MRNA].
RA Bollen A., Gobert J., Wuelfert E.;
RT "Expression of human proapolipoprotein A-1.";
RL Patent number EP0293357, 30-NOV-1988.
RN [12]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Testis;
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H.,
RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y.,
RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [13]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RG NHLBI resequencing and genotyping service (RS&G);
RL Submitted (FEB-2007) to the EMBL/GenBank/DDBJ databases.
RN [14]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M.,
RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA Hunkapiller M.W., Myers E.W., Venter J.C.;
RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [15]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Brain, and Skeletal muscle;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [16]
RP PROTEIN SEQUENCE OF 19-27.
RX PubMed=6409108; DOI=10.1016/0006-291x(83)91772-2;
RA Brewer H.B. Jr., Fairwell T., Kay L., Meng M., Ronan R., Law S.,
RA Light J.A.;
RT "Human plasma proapoA-I: isolation and amino-terminal sequence.";
RL Biochem. Biophys. Res. Commun. 113:626-632(1983).
RN [17]
RP PROTEIN SEQUENCE OF 25-267.
RX PubMed=164450; DOI=10.1016/s0021-9258(19)41662-1;
RA Baker H.N., Gotto A.M. Jr., Jackson R.L.;
RT "The primary structure of human plasma high density apolipoprotein
RT glutamine I (ApoA-I). II. The amino acid sequence and alignment of cyanogen
RT bromide fragments IV, III, and I.";
RL J. Biol. Chem. 250:2725-2738(1975).
RN [18]
RP PROTEIN SEQUENCE OF 25-267.
RX PubMed=204308; DOI=10.1016/0006-291x(78)91614-5;
RA Brewer H.B. Jr., Fairwell T., Larue A., Ronan R., Houser A., Bronzert T.J.;
RT "The amino acid sequence of human APOA-I, an apolipoprotein isolated from
RT high density lipoproteins.";
RL Biochem. Biophys. Res. Commun. 80:623-630(1978).
RN [19]
RP PROTEIN SEQUENCE OF 25-56.
RX PubMed=3047170; DOI=10.1172/jci113682;
RA Yui Y., Aoyama T., Morishita H., Takahashi M., Takatsu Y., Kawai C.;
RT "Serum prostacyclin stabilizing factor is identical to apolipoprotein A-I
RT (Apo A-I). A novel function of Apo A-I.";
RL J. Clin. Invest. 82:803-807(1988).
RN [20]
RP PROTEIN SEQUENCE OF 25-50, FUNCTION, AND IDENTIFICATION IN THE SPAP
RP COMPLEX.
RC TISSUE=Serum;
RX PubMed=1909888; DOI=10.1021/bi00101a011;
RA Aakerloef E., Joernvall H., Slotte H., Pousette A.;
RT "Identification of apolipoprotein A1 and immunoglobulin as components of a
RT serum complex that mediates activation of human sperm motility.";
RL Biochemistry 30:8986-8990(1991).
RN [21]
RP PROTEIN SEQUENCE OF 25-48.
RX PubMed=2506184; DOI=10.1016/s0021-9258(19)84784-1;
RA Manjunath P., Marcel Y.L., Uma J., Seidah N.G., Chretien M.,
RA Chapdelaine A.;
RT "Apolipoprotein A-I binds to a family of bovine seminal plasma proteins.";
RL J. Biol. Chem. 264:16853-16857(1989).
RN [22]
RP PROTEIN SEQUENCE OF 25-43.
RX PubMed=3120314; DOI=10.1126/science.3120314;
RA Prioli R.P., Ordovas J.M., Rosenberg I., Schaeffer E.J., Pereira M.E.A.;
RT "Similarity of cruzin, an inhibitor of Trypanosoma cruzi neuraminidase, to
RT high-density lipoprotein.";
RL Science 238:1417-1419(1987).
RN [23]
RP PROTEIN SEQUENCE OF 25-42.
RC TISSUE=Heart;
RX PubMed=7895732; DOI=10.1002/elps.11501501209;
RA Corbett J.M., Wheeler C.H., Baker C.S., Yacoub M.H., Dunn M.J.;
RT "The human myocardial two-dimensional gel protein database: update 1994.";
RL Electrophoresis 15:1459-1465(1994).
RN [24]
RP PROTEIN SEQUENCE OF 25-34.
RC TISSUE=Platelet;
RX PubMed=12665801; DOI=10.1038/nbt810;
RA Gevaert K., Goethals M., Martens L., Van Damme J., Staes A., Thomas G.R.,
RA Vandekerckhove J.;
RT "Exploring proteomes and analyzing protein processing by mass spectrometric
RT identification of sorted N-terminal peptides.";
RL Nat. Biotechnol. 21:566-569(2003).
RN [25]
RP PROTEIN SEQUENCE OF 25-33, AND INTERACTION WITH NAXE AND CLU.
RX PubMed=1742316; DOI=10.1016/0005-2760(91)90167-g;
RA Ehnholm C., Bozas S.E., Tenkanen H., Kirszbaum L., Metso J., Murphy B.,
RA Walker I.D.;
RT "The apolipoprotein A-I binding protein of placenta and the SP-40,40
RT protein of human blood are different proteins which both bind to
RT apolipoprotein A-I.";
RL Biochim. Biophys. Acta 1086:255-260(1991).
RN [26]
RP PROTEIN SEQUENCE OF 35-64; 70-101; 121-140; 165-173; 185-195 AND 240-263,
RP AND IDENTIFICATION BY MASS SPECTROMETRY.
RC TISSUE=Brain, Cajal-Retzius cell, and Fetal brain cortex;
RA Lubec G., Vishwanath V., Chen W.-Q., Sun Y.;
RL Submitted (DEC-2008) to UniProtKB.
RN [27]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 118-267.
RX PubMed=6294659; DOI=10.1073/pnas.79.22.6861;
RA Breslow J.L., Ross D., McPherson J., Williams H.W., Kurnit D.,
RA Nussbaum A.L., Karathanasis S.K., Zannis V.I.;
RT "Isolation and characterization of cDNA clones for human apolipoprotein A-
RT I.";
RL Proc. Natl. Acad. Sci. U.S.A. 79:6861-6865(1982).
RN [28]
RP PALMITOYLATION.
RX PubMed=3005308; DOI=10.1016/s0021-9258(17)35598-9;
RA Hoeg J.M., Meng M.S., Ronan R., Fairwell T., Brewer H.B. Jr.;
RT "Human apolipoprotein A-I. Post-translational modification by fatty acid
RT acylation.";
RL J. Biol. Chem. 261:3911-3914(1986).
RN [29]
RP PROTEOLYTIC PROCESSING.
RX PubMed=6405383; DOI=10.1073/pnas.80.9.2574;
RA Zannis V.I., Karathanasis S.K., Keutmann H.T., Goldberger G., Breslow J.L.;
RT "Intracellular and extracellular processing of human apolipoprotein A-I:
RT secreted apolipoprotein A-I isoprotein 2 is a propeptide.";
RL Proc. Natl. Acad. Sci. U.S.A. 80:2574-2578(1983).
RN [30]
RP INVOLVEMENT IN FHA2.
RX PubMed=1898657; DOI=10.1172/jci114997;
RA Funke H., von Eckardstein A., Pritchard P.H., Karas M., Albers J.J.,
RA Assmann G.;
RT "A frameshift mutation in the human apolipoprotein A-I gene causes high
RT density lipoprotein deficiency, partial lecithin: cholesterol-
RT acyltransferase deficiency, and corneal opacities.";
RL J. Clin. Invest. 87:371-376(1991).
RN [31]
RP GLYCATION AT LYS-263.
RX PubMed=8261628; DOI=10.1016/0009-8981(93)90165-z;
RA Calvo C., Ulloa N., Campos M., Verdugo C., Ayrault-Jarrier M.;
RT "The preferential site of non-enzymatic glycation of human apolipoprotein
RT A-I in vivo.";
RL Clin. Chim. Acta 217:193-198(1993).
RN [32]
RP INTERACTION WITH NAXE.
RX PubMed=11991719; DOI=10.1006/geno.2002.6761;
RA Ritter M., Buechler C., Boettcher A., Barlage S., Schmitz-Madry A.,
RA Orso E., Bared S.M., Schmiedeknecht G., Baehr C.H., Fricker G., Schmitz G.;
RT "Cloning and characterization of a novel apolipoprotein A-I-binding
RT protein, AI-BP, secreted by cells of the kidney proximal tubules in
RT response to HDL or ApoA-I.";
RL Genomics 79:693-702(2002).
RN [33]
RP INTERACTION WITH SCGB3A2.
RX PubMed=12847263; DOI=10.4049/jimmunol.171.2.924;
RA Bin L.H., Nielson L.D., Liu X., Mason R.J., Shu H.B.;
RT "Identification of uteroglobin-related protein 1 and macrophage scavenger
RT receptor with collagenous structure as a lung-specific ligand-receptor
RT pair.";
RL J. Immunol. 171:924-930(2003).
RN [34]
RP MASS SPECTROMETRY, OXIDATION AT MET-110 AND MET-136, AND TISSUE
RP SPECIFICITY.
RX PubMed=12576517; DOI=10.1194/jlr.m200256-jlr200;
RA Pankhurst G., Wang X.L., Wilcken D.E., Baernthaler G., Panzenboeck U.,
RA Raftery M., Stocker R.;
RT "Characterization of specifically oxidized apolipoproteins in mildly
RT oxidized high density lipoprotein.";
RL J. Lipid Res. 44:349-355(2003).
RN [35]
RP IDENTIFICATION BY MASS SPECTROMETRY.
RX PubMed=12562854; DOI=10.1194/jlr.d200034-jlr200;
RA Niederkofler E.E., Tubbs K.A., Kiernan U.A., Nedelkov D., Nelson R.W.;
RT "Novel mass spectrometric immunoassays for the rapid structural
RT characterization of plasma apolipoproteins.";
RL J. Lipid Res. 44:630-639(2003).
RN [36]
RP INTERACTION WITH NDRG1.
RX PubMed=15922294; DOI=10.1016/j.bbrc.2005.05.050;
RA Hunter M., Angelicheva D., Tournev I., Ingley E., Chan D.C., Watts G.F.,
RA Kremensky I., Kalaydjieva L.;
RT "NDRG1 interacts with APO A-I and A-II and is a functional candidate for
RT the HDL-C QTL on 8q24.";
RL Biochem. Biophys. Res. Commun. 332:982-992(2005).
RN [37]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T.,
RA Bennett K.L., Superti-Furga G., Colinge J.;
RT "Initial characterization of the human central proteome.";
RL BMC Syst. Biol. 5:17-17(2011).
RN [38]
RP INTERACTION WITH NAXE AND YJEFN3.
RX PubMed=23719382; DOI=10.1038/nature12166;
RA Fang L., Choi S.H., Baek J.S., Liu C., Almazan F., Ulrich F., Wiesner P.,
RA Taleb A., Deer E., Pattison J., Torres-Vazquez J., Li A.C., Miller Y.I.;
RT "Control of angiogenesis by AIBP-mediated cholesterol efflux.";
RL Nature 498:118-122(2013).
RN [39]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
RA Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L.,
RA Ye M., Zou H.;
RT "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver
RT phosphoproteome.";
RL J. Proteomics 96:253-262(2014).
RN [40]
RP CHARACTERIZATION OF VARIANT MILANO CYS-197.
RX PubMed=24755625; DOI=10.1371/journal.pone.0096150;
RA Petrlova J., Dalla-Riva J., Morgelin M., Lindahl M., Krupinska E.,
RA Stenkula K.G., Voss J.C., Lagerstedt J.O.;
RT "Secondary structure changes in ApoA-I Milano (R173C) are not accompanied
RT by a decrease in protein stability or solubility.";
RL PLoS ONE 9:E96150-E96150(2014).
RN [41]
RP STRUCTURE BY NMR OF 190-209.
RX PubMed=8664326; DOI=10.1016/0005-2760(96)00037-9;
RA Wang G., Treleaven W.D., Cushley R.J.;
RT "Conformation of human serum apolipoprotein A-I(166-185) in the presence of
RT sodium dodecyl sulfate or dodecylphosphocholine by 1H-NMR and CD. Evidence
RT for specific peptide-SDS interactions.";
RL Biochim. Biophys. Acta 1301:174-184(1996).
RN [42]
RP X-RAY CRYSTALLOGRAPHY (4.0 ANGSTROMS) OF 67-267.
RX PubMed=9356442; DOI=10.1073/pnas.94.23.12291;
RA Borhani D.W., Rogers D.P., Engler J.A., Brouillette C.G.;
RT "Crystal structure of truncated human apolipoprotein A-I suggests a lipid-
RT bound conformation.";
RL Proc. Natl. Acad. Sci. U.S.A. 94:12291-12296(1997).
RN [43]
RP DISEASE.
RX PubMed=8240372; DOI=10.1006/bbrc.1993.2341;
RA Nakata K., Kobayashi K., Yanagi H., Shimakura Y., Tsuchiya S., Arinami T.,
RA Hamaguchi H.;
RT "Autosomal dominant hypoalphalipoproteinemia due to a completely defective
RT apolipoprotein A-I gene.";
RL Biochem. Biophys. Res. Commun. 196:950-955(1993).
RN [44]
RP INVOLVEMENT IN FHA2, VARIANT FHA2 23-GLN--GLN-267 DEL, AND CHARACTERIZATION
RP OF VARIANT FHA2 23-GLN--GLN-267 DEL.
RX PubMed=8282791; DOI=10.1172/jci116949;
RA Ng D.S., Leiter L.A., Vezina C., Connelly P.W., Hegele R.A.;
RT "Apolipoprotein A-I Q[-2]X causing isolated apolipoprotein A-I deficiency
RT in a family with analphalipoproteinemia.";
RL J. Clin. Invest. 93:223-229(1994).
RN [45]
RP VARIANT MILANO CYS-197.
RX PubMed=6401735; DOI=10.1016/s0021-9258(18)32955-7;
RA Weisgraber K.H., Rall S.C. Jr., Bersot T.P., Mahley R.W., Franceschini G.,
RA Sirtori C.R.;
RT "Apolipoprotein A-IMilano. Detection of normal A-I in affected subjects and
RT evidence for a cysteine for arginine substitution in the variant A-I.";
RL J. Biol. Chem. 258:2508-2513(1983).
RN [46]
RP VARIANT TANGIER.
RX PubMed=6412234; DOI=10.1073/pnas.80.19.6081;
RA Schmitz G., Assmann G., Rall S.C. Jr., Mahley R.W.;
RT "Tangier disease: defective recombination of a specific Tangier
RT apolipoprotein A-I isoform (pro-apo A-I) with high density lipoproteins.";
RL Proc. Natl. Acad. Sci. U.S.A. 80:6081-6085(1983).
RN [47]
RP VARIANT GIESSEN ARG-167.
RX PubMed=6489332; DOI=10.1111/j.1432-1033.1984.tb08467.x;
RA Utermann G., Haas J., Steinmetz A., Paetzold R., Rall S.C. Jr.,
RA Weisgraber K.H., Mahley R.W.;
RT "Apolipoprotein A-IGiessen (Pro143-->Arg). A mutant that is defective in
RT activating lecithin:cholesterol acyltransferase.";
RL Eur. J. Biochem. 144:325-331(1984).
RN [48]
RP VARIANT NORWAY LYS-160.
RX PubMed=6432779; DOI=10.1016/s0021-9258(18)90928-2;
RA Rall S.C. Jr., Weisgraber K.H., Mahley R.W., Ogawa Y., Fielding C.J.,
RA Utermann G., Haas J., Steinmetz A., Menzel H.J., Assmann G.;
RT "Abnormal lecithin:cholesterol acyltransferase activation by a human
RT apolipoprotein A-I variant in which a single lysine residue is deleted.";
RL J. Biol. Chem. 259:10063-10070(1984).
RN [49]
RP PROTEIN SEQUENCE OF 25-107, AND VARIANT AMYL8 ARG-50.
RX PubMed=3142462; DOI=10.1016/s0006-291x(88)80909-4;
RA Nichols W.C., Dwulet F.E., Liepnieks J., Benson M.D.;
RT "Variant apolipoprotein AI as a major constituent of a human hereditary
RT amyloid.";
RL Biochem. Biophys. Res. Commun. 156:762-768(1988).
RN [50]
RP VARIANT AMYL8 ARG-50.
RX PubMed=2123470; DOI=10.1016/0888-7543(90)90288-6;
RA Nichols W.C., Gregg R.E., Brewer H.B. Jr., Benson M.D.;
RT "A mutation in apolipoprotein A-I in the Iowa type of familial amyloidotic
RT polyneuropathy.";
RL Genomics 8:318-323(1990).
RN [51]
RP PROTEIN SEQUENCE OF 25-267, AND VARIANT FUKUOKA LYS-134.
RX PubMed=2107878; DOI=10.1016/0005-2760(90)90292-6;
RA Takada Y., Sasaki J., Ogata S., Nakanishi T., Ikehara Y., Arakawa K.;
RT "Isolation and characterization of human apolipoprotein A-I Fukuoka (110
RT Glu-->Lys). A novel apolipoprotein variant.";
RL Biochim. Biophys. Acta 1043:169-176(1990).
RN [52]
RP PROTEIN SEQUENCE OF 25-112, AND VARIANT AMYL8 ARG-84.
RX PubMed=1502149; DOI=10.1073/pnas.89.16.7389;
RA Soutar A.K., Hawkins P.N., Vigushin D.M., Tennent G.A., Booth S.E.,
RA Hutton T., Nguyen O., Totty N.F., Feest T.G., Hsuan J.J., Pepys M.B.;
RT "Apolipoprotein AI mutation Arg-60 causes autosomal dominant amyloidosis.";
RL Proc. Natl. Acad. Sci. U.S.A. 89:7389-7393(1992).
RN [53]
RP VARIANT BALTIMORE LEU-34.
RX PubMed=2108924; DOI=10.1007/bf00195816;
RA Ladias J.A.A., Kwiterovich P.O. Jr., Smith H.H., Karathanasis S.K.,
RA Antonarakis S.E.;
RT "Apolipoprotein A1 Baltimore (Arg-10-->Leu), a new ApoA1 variant.";
RL Hum. Genet. 84:439-445(1990).
RN [54]
RP VARIANTS ARG-27; ARG-28 AND ARG-189.
RX PubMed=2512329; DOI=10.1172/jci114355;
RA von Eckardstein A., Funke H., Henke A., Altland K., Benninghoven A.,
RA Assmann G., Welp S., Roetrige A., Kock R.;
RT "Apolipoprotein A-I variants. Naturally occurring substitutions of proline
RT residues affect plasma concentration of apolipoprotein A-I.";
RL J. Clin. Invest. 84:1722-1730(1989).
RN [55]
RP VARIANTS GLU-113; MET-131; GLY-163; VAL-171 AND LYS-222.
RX PubMed=2111322; DOI=10.1016/s0021-9258(19)38931-8;
RA von Eckardstein A., Funke H., Walter M., Altland K., Benninghoven A.,
RA Assmann G.;
RT "Structural analysis of human apolipoprotein A-I variants. Amino acid
RT substitutions are nonrandomly distributed throughout the apolipoprotein A-I
RT primary structure.";
RL J. Biol. Chem. 265:8610-8617(1990).
RN [56]
RP VARIANT FHA2 108-GLN--GLN-267 DEL, CHARACTERIZATION OF VARIANT FHA2
RP 108-GLN--GLN-267 DEL, AND VARIANT THR-61.
RX PubMed=1901417; DOI=10.1073/pnas.88.7.2793;
RA Matsunaga T., Hiasa Y., Yanagi H., Maeda T., Hattori N., Yamakawa K.,
RA Yamanouchi Y., Tanaka I., Obara T., Hamaguchi H.;
RT "Apolipoprotein A-I deficiency due to a codon 84 nonsense mutation of the
RT apolipoprotein A-I gene.";
RL Proc. Natl. Acad. Sci. U.S.A. 88:2793-2797(1991).
RN [57]
RP VARIANT HDL DEFICIENCY 56-GLN--GLN-267 DEL, AND CHARACTERIZATION OF VARIANT
RP HDL DEFICIENCY 56-GLN--GLN-267 DEL.
RX PubMed=7981179; DOI=10.1161/01.atv.14.12.1915;
RA Roemling R., von Eckardstein A., Funke H., Motti C., Fragiacomo G.C.,
RA Noseda G., Assmann G.;
RT "A nonsense mutation in the apolipoprotein A-I gene is associated with
RT high-density lipoprotein deficiency and periorbital xanthelasmas.";
RL Arterioscler. Thromb. 14:1915-1922(1994).
RN [58]
RP VARIANTS HITA AND TSUSHIMA.
RX PubMed=7918609;
RA Araki K., Sasaki J., Matsunaga A., Takada Y., Moriyama K., Hidaka K.,
RA Arakawa K.;
RT "Characterization of two new human apolipoprotein A-I variants:
RT apolipoprotein A-I Tsushima (Trp-108-->Arg) and A-I Hita (Ala-95-->Asp).";
RL Biochim. Biophys. Acta 1214:272-278(1994).
RN [59]
RP VARIANT AMYL8 ARG-50.
RX PubMed=8208902;
RA Vigushin D.M., Gough J., Allan D., Alguacil A., Penner B., Pettigrew N.M.,
RA Quinonez G., Bernstein K., Booth S.E., Booth D.R., Soutar A.K.,
RA Hawkins P.N., Pepys M.B.;
RT "Familial nephropathic systemic amyloidosis caused by apolipoprotein AI
RT variant Arg26.";
RL Q. J. Med. 87:149-154(1994).
RN [60]
RP VARIANT AMYL8 SER-198, AND CHARACTERIZATION OF VARIANT AMYL8 SER-198.
RX PubMed=10487826; DOI=10.1016/s0002-9440(10)65167-x;
RA Obici L., Bellotti V., Mangione P., Stoppini M., Arbustini E., Verga L.,
RA Zorzoli I., Anesi E., Zanotti G., Campana C., Vigano M., Merlini G.;
RT "The new apolipoprotein A-I variant leu(174) --> Ser causes hereditary
RT cardiac amyloidosis, and the amyloid fibrils are constituted by the 93-
RT residue N-terminal polypeptide.";
RL Am. J. Pathol. 155:695-702(1999).
RN [61]
RP VARIANT AOITA GLU-180.
RX PubMed=9514407; DOI=10.1161/01.atv.18.3.389;
RA Huang W., Sasaki J., Matsunaga A., Nanimatsu H., Moriyama K., Han H.,
RA Kugi M., Koga T., Yamaguchi K., Arakawa K.;
RT "A novel homozygous missense mutation in the apo A-I gene with apo A-I
RT deficiency.";
RL Arterioscler. Thromb. Vasc. Biol. 18:389-396(1998).
RN [62]
RP VARIANT ZARAGOZA ARG-168.
RA Recalde D., Cenarro A., Civeira F., Pocovi M.;
RT "Apo A-I Zaragoza(L144R): a novel mutation in the apolipoprotein A-I gene
RT associated with familial hypoalphalipoproteinemia.";
RL Hum. Mutat. 11:416-416(1998).
RN [63]
RP VARIANT AMYL8 PRO-173.
RX PubMed=10198255; DOI=10.1006/bbrc.1999.0518;
RA Hamidi Asl K., Liepnieks J.J., Nakamura M., Parker F., Benson M.D.;
RT "A novel apolipoprotein A-1 variant, Arg173Pro, associated with cardiac and
RT cutaneous amyloidosis.";
RL Biochem. Biophys. Res. Commun. 257:584-588(1999).
RN [64]
RP VARIANTS AMYL8 ARG-50 AND PRO-199.
RX PubMed=12050338; DOI=10.1056/nejmoa013354;
RA Lachmann H.J., Booth D.R., Booth S.E., Bybee A., Gilbertson J.A.,
RA Gillmore J.D., Pepys M.B., Hawkins P.N.;
RT "Misdiagnosis of hereditary amyloidosis as AL (primary) amyloidosis.";
RL N. Engl. J. Med. 346:1786-1791(2002).
RN [65]
RP VARIANT ILE-92.
RX PubMed=12966036; DOI=10.1093/hmg/ddg314;
RA Morabia A., Cayanis E., Costanza M.C., Ross B.M., Flaherty M.S.,
RA Alvin G.B., Das K., Gilliam T.C.;
RT "Association of extreme blood lipid profile phenotypic variation with 11
RT reverse cholesterol transport genes and 10 non-genetic cardiovascular
RT disease risk factors.";
RL Hum. Mol. Genet. 12:2733-2743(2003).
RN [66]
RP VARIANT ILE-92, AND IDENTIFICATION BY MASS SPECTROMETRY.
RX PubMed=22028381; DOI=10.1093/jmcb/mjr024;
RA Su Z.D., Sun L., Yu D.X., Li R.X., Li H.X., Yu Z.J., Sheng Q.H., Lin X.,
RA Zeng R., Wu J.R.;
RT "Quantitative detection of single amino acid polymorphisms by targeted
RT proteomics.";
RL J. Mol. Cell Biol. 3:309-315(2011).
RN [67]
RP VARIANT BOSTON SER-173.
RX PubMed=26073399; DOI=10.1016/j.jacl.2015.02.005;
RA Anthanont P., Asztalos B.F., Polisecki E., Zachariah B., Schaefer E.J.;
RT "Case report: A novel apolipoprotein A-I missense mutation apoA-I
RT (Arg149Ser)Boston associated with decreased lecithin-cholesterol
RT acyltransferase activation and cellular cholesterol efflux.";
RL J. Clin. Lipidol. 9:390-395(2015).
CC -!- FUNCTION: Participates in the reverse transport of cholesterol from
CC tissues to the liver for excretion by promoting cholesterol efflux from
CC tissues and by acting as a cofactor for the lecithin cholesterol
CC acyltransferase (LCAT). As part of the SPAP complex, activates
CC spermatozoa motility. {ECO:0000269|PubMed:1909888}.
CC -!- SUBUNIT: Homodimer (By similarity). Interacts with NAXE and CLU
CC (PubMed:1742316, PubMed:11991719). Component of a sperm activating
CC protein complex (SPAP), consisting of APOA1, an immunoglobulin heavy
CC chain, an immunoglobulin light chain and albumin (PubMed:1909888).
CC Interacts with NDRG1 (PubMed:15922294). Interacts with SCGB3A2
CC (PubMed:12847263). Interacts with NAXE and YJEFN3 (PubMed:23719382).
CC {ECO:0000250|UniProtKB:G5BQH5, ECO:0000269|PubMed:11991719,
CC ECO:0000269|PubMed:12847263, ECO:0000269|PubMed:15922294,
CC ECO:0000269|PubMed:1742316, ECO:0000269|PubMed:1909888,
CC ECO:0000269|PubMed:23719382}.
CC -!- INTERACTION:
CC P02647; O95477: ABCA1; NbExp=8; IntAct=EBI-701692, EBI-784112;
CC P02647; P02647: APOA1; NbExp=28; IntAct=EBI-701692, EBI-701692;
CC P02647; P05067: APP; NbExp=8; IntAct=EBI-701692, EBI-77613;
CC P02647; Q07021: C1QBP; NbExp=2; IntAct=EBI-701692, EBI-347528;
CC P02647; Q96DZ9: CMTM5; NbExp=3; IntAct=EBI-701692, EBI-2548702;
CC P02647; Q96DZ9-2: CMTM5; NbExp=6; IntAct=EBI-701692, EBI-11522780;
CC P02647; P00738: HP; NbExp=3; IntAct=EBI-701692, EBI-1220767;
CC P02647; P13473-2: LAMP2; NbExp=3; IntAct=EBI-701692, EBI-21591415;
CC P02647; P04180: LCAT; NbExp=2; IntAct=EBI-701692, EBI-9104464;
CC P02647; Q9Y371: SH3GLB1; NbExp=3; IntAct=EBI-701692, EBI-2623095;
CC P02647; P37840: SNCA; NbExp=3; IntAct=EBI-701692, EBI-985879;
CC -!- SUBCELLULAR LOCATION: Secreted.
CC -!- TISSUE SPECIFICITY: Major protein of plasma HDL, also found in
CC chylomicrons. Synthesized in the liver and small intestine. The
CC oxidized form at Met-110 and Met-136 is increased in individuals with
CC increased risk for coronary artery disease, such as in carrier of the
CC eNOSa/b genotype and exposure to cigarette smoking. It is also present
CC in increased levels in aortic lesions relative to native ApoA-I and
CC increased levels are seen with increasing severity of disease.
CC {ECO:0000269|PubMed:12576517}.
CC -!- PTM: Glycosylated. {ECO:0000250}.
CC -!- PTM: Palmitoylated. {ECO:0000269|PubMed:3005308}.
CC -!- PTM: Phosphorylation sites are present in the extracellular medium.
CC -!- MASS SPECTROMETRY: [Apolipoprotein A-I]: Mass=28081;
CC Method=Electrospray; Note=Without methionine sulfoxide.;
CC Evidence={ECO:0000269|PubMed:12576517};
CC -!- MASS SPECTROMETRY: [Apolipoprotein A-I]: Mass=28098;
CC Method=Electrospray; Note=With 1 methionine sulfoxide, oxidation at
CC Met-110.; Evidence={ECO:0000269|PubMed:12576517};
CC -!- MASS SPECTROMETRY: [Apolipoprotein A-I]: Mass=28095;
CC Method=Electrospray; Note=With 1 methionine sulfoxide, oxidation at
CC Met-136.; Evidence={ECO:0000269|PubMed:12576517};
CC -!- MASS SPECTROMETRY: [Apolipoprotein A-I]: Mass=28114;
CC Method=Electrospray; Note=With 2 methionine sulfoxides, oxidation at
CC Met-110 and Met-136.; Evidence={ECO:0000269|PubMed:12576517};
CC -!- POLYMORPHISM: Genetic variations in APOA1 can result in APOA1
CC deficiency and are associated with low levels of HDL cholesterol
CC [MIM:107680]. {ECO:0000305}.
CC -!- DISEASE: Hypoalphalipoproteinemia, primary, 2 (FHA2) [MIM:618463]: A
CC rare disorder of lipoprotein metabolism, biochemically characterized by
CC complete or partial apoA-I deficiency and mild to severe reduction of
CC serum high-density lipoprotein cholesterol (HDL-C). Severe
CC hypoalphalipoproteinemia characterized by undetectable levels of apoA-I
CC is an autosomal recessive condition, generally associated with markedly
CC increased atherosclerotic cardiovascular disease, xanthomas and corneal
CC opacities. Mild hypoalphalipoproteinemia characterized by half the
CC normal plasma apoA-I and HDL-C levels is inherited as an autosomal
CC dominant trait, may be associated with xanthomas and corneal opacities,
CC but most patients do not have increased cardiovascular risk.
CC {ECO:0000269|PubMed:1898657, ECO:0000269|PubMed:1901417,
CC ECO:0000269|PubMed:8282791}. Note=The disease is caused by variants
CC affecting the gene represented in this entry.
CC -!- DISEASE: Note=APOA1 mutations may be involved in the pathogenesis of
CC amyloid polyneuropathy-nephropathy Iowa type, also known as amyloidosis
CC van Allen type or familial amyloid polyneuropathy type III
CC (PubMed:3142462 and PubMed:2123470). The clinical picture is dominated
CC by neuropathy in the early stages of the disease and nephropathy late
CC in the course. Death is due in most cases to renal amyloidosis.
CC -!- DISEASE: Amyloidosis 8 (AMYL8) [MIM:105200]: A form of hereditary
CC generalized amyloidosis. Clinical features include extensive visceral
CC amyloid deposits, renal amyloidosis resulting in nephrotic syndrome,
CC arterial hypertension, hepatosplenomegaly, cholestasis, petechial skin
CC rash. There is no involvement of the nervous system.
CC {ECO:0000269|PubMed:10198255, ECO:0000269|PubMed:10487826,
CC ECO:0000269|PubMed:12050338, ECO:0000269|PubMed:1502149,
CC ECO:0000269|PubMed:2123470, ECO:0000269|PubMed:3142462,
CC ECO:0000269|PubMed:8208902}. Note=The disease is caused by variants
CC affecting the gene represented in this entry.
CC -!- SIMILARITY: Belongs to the apolipoprotein A1/A4/E family.
CC {ECO:0000305}.
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DR EMBL; J00098; AAB59514.1; -; Genomic_DNA.
DR EMBL; X01038; CAA25519.1; -; Genomic_DNA.
DR EMBL; X02162; CAA26097.1; -; mRNA.
DR EMBL; X00566; CAA25232.1; -; mRNA.
DR EMBL; M11791; AAA35545.1; -; mRNA.
DR EMBL; X07496; CAA30377.1; -; Genomic_DNA.
DR EMBL; M27875; AAA62829.1; -; mRNA.
DR EMBL; M29068; AAA51747.1; -; mRNA.
DR EMBL; AY422952; AAQ91811.1; -; Genomic_DNA.
DR EMBL; AY555191; AAS68227.1; -; Genomic_DNA.
DR EMBL; A14829; CAA01198.1; -; mRNA.
DR EMBL; AK292231; BAF84920.1; -; mRNA.
DR EMBL; EF444948; ACA05932.1; -; Genomic_DNA.
DR EMBL; EF444948; ACA05933.1; -; Genomic_DNA.
DR EMBL; EF444948; ACA05934.1; -; Genomic_DNA.
DR EMBL; EF444948; ACA05935.1; -; Genomic_DNA.
DR EMBL; EF444948; ACA05936.1; -; Genomic_DNA.
DR EMBL; CH471065; EAW67274.1; -; Genomic_DNA.
DR EMBL; BC005380; AAH05380.1; -; mRNA.
DR EMBL; BC110286; AAI10287.1; -; mRNA.
DR CCDS; CCDS8378.1; -.
DR PIR; A90947; LPHUA1.
DR RefSeq; NP_000030.1; NM_000039.2.
DR RefSeq; NP_001304946.1; NM_001318017.1.
DR RefSeq; NP_001304947.1; NM_001318018.1.
DR RefSeq; NP_001304950.1; NM_001318021.1.
DR PDB; 1AV1; X-ray; 4.00 A; A/B/C/D=68-267.
DR PDB; 1GW3; NMR; -; A=166-211.
DR PDB; 1GW4; NMR; -; A=166-211.
DR PDB; 1ODP; NMR; -; A=190-209.
DR PDB; 1ODQ; NMR; -; A=190-209.
DR PDB; 1ODR; NMR; -; A=190-209.
DR PDB; 2MSC; NMR; -; A/C=68-265.
DR PDB; 2MSD; NMR; -; A/C=68-265.
DR PDB; 2MSE; NMR; -; A/C=68-265.
DR PDB; 2N5E; NMR; -; A/B=79-267.
DR PDB; 3K2S; X-ray; -; A/B=25-267.
DR PDB; 3R2P; X-ray; 2.20 A; A=25-208.
DR PDB; 4V6M; EM; 7.10 A; A0/A1=68-267.
DR PDB; 6CC9; NMR; -; A/C=68-265.
DR PDB; 6CCH; NMR; -; A/C=68-265.
DR PDB; 6CCX; NMR; -; A/C=68-265.
DR PDB; 6CLZ; NMR; -; B/C=79-267.
DR PDB; 6CM1; NMR; -; B/C=79-267.
DR PDB; 6PTS; NMR; -; A/C=68-265.
DR PDB; 6PTW; NMR; -; A/C=68-265.
DR PDB; 6W4E; NMR; -; A/D=68-265.
DR PDB; 6W4F; NMR; -; A/D=68-265.
DR PDB; 7KJR; EM; 2.08 A; C/D=79-267.
DR PDB; 7RSC; NMR; -; D/E=68-265.
DR PDB; 7RSE; NMR; -; D/E=68-265.
DR PDBsum; 1AV1; -.
DR PDBsum; 1GW3; -.
DR PDBsum; 1GW4; -.
DR PDBsum; 1ODP; -.
DR PDBsum; 1ODQ; -.
DR PDBsum; 1ODR; -.
DR PDBsum; 2MSC; -.
DR PDBsum; 2MSD; -.
DR PDBsum; 2MSE; -.
DR PDBsum; 2N5E; -.
DR PDBsum; 3K2S; -.
DR PDBsum; 3R2P; -.
DR PDBsum; 4V6M; -.
DR PDBsum; 6CC9; -.
DR PDBsum; 6CCH; -.
DR PDBsum; 6CCX; -.
DR PDBsum; 6CLZ; -.
DR PDBsum; 6CM1; -.
DR PDBsum; 6PTS; -.
DR PDBsum; 6PTW; -.
DR PDBsum; 6W4E; -.
DR PDBsum; 6W4F; -.
DR PDBsum; 7KJR; -.
DR PDBsum; 7RSC; -.
DR PDBsum; 7RSE; -.
DR AlphaFoldDB; P02647; -.
DR BMRB; P02647; -.
DR SMR; P02647; -.
DR BioGRID; 106832; 174.
DR CORUM; P02647; -.
DR DIP; DIP-29619N; -.
DR IntAct; P02647; 93.
DR MINT; P02647; -.
DR STRING; 9606.ENSP00000236850; -.
DR ChEMBL; CHEMBL5984; -.
DR DrugBank; DB09130; Copper.
DR DrugBank; DB11886; Infigratinib.
DR DrugBank; DB00877; Sirolimus.
DR DrugBank; DB01593; Zinc.
DR DrugBank; DB14487; Zinc acetate.
DR DrugBank; DB14533; Zinc chloride.
DR DrugBank; DB14548; Zinc sulfate, unspecified form.
DR CarbonylDB; P02647; -.
DR GlyGen; P02647; 1 site, 1 O-linked glycan (1 site).
DR iPTMnet; P02647; -.
DR MetOSite; P02647; -.
DR PhosphoSitePlus; P02647; -.
DR BioMuta; APOA1; -.
DR DMDM; 113992; -.
DR DOSAC-COBS-2DPAGE; P02647; -.
DR OGP; P02647; -.
DR REPRODUCTION-2DPAGE; IPI00021841; -.
DR REPRODUCTION-2DPAGE; P02647; -.
DR SWISS-2DPAGE; P02647; -.
DR UCD-2DPAGE; P02647; -.
DR CPTAC; non-CPTAC-1075; -.
DR CPTAC; non-CPTAC-1076; -.
DR EPD; P02647; -.
DR jPOST; P02647; -.
DR MassIVE; P02647; -.
DR MaxQB; P02647; -.
DR PaxDb; P02647; -.
DR PeptideAtlas; P02647; -.
DR PRIDE; P02647; -.
DR ProteomicsDB; 51536; -.
DR TopDownProteomics; P02647; -.
DR ABCD; P02647; 1 sequenced antibody.
DR Antibodypedia; 32291; 1593 antibodies from 48 providers.
DR DNASU; 335; -.
DR Ensembl; ENST00000236850.5; ENSP00000236850.3; ENSG00000118137.10.
DR Ensembl; ENST00000359492.6; ENSP00000352471.2; ENSG00000118137.10.
DR Ensembl; ENST00000375320.5; ENSP00000364469.1; ENSG00000118137.10.
DR Ensembl; ENST00000375323.5; ENSP00000364472.1; ENSG00000118137.10.
DR GeneID; 335; -.
DR KEGG; hsa:335; -.
DR MANE-Select; ENST00000236850.5; ENSP00000236850.3; NM_000039.3; NP_000030.1.
DR UCSC; uc001ppv.2; human.
DR CTD; 335; -.
DR DisGeNET; 335; -.
DR GeneCards; APOA1; -.
DR HGNC; HGNC:600; APOA1.
DR HPA; ENSG00000118137; Tissue enriched (liver).
DR MalaCards; APOA1; -.
DR MIM; 105200; phenotype.
DR MIM; 107680; gene.
DR MIM; 618463; phenotype.
DR neXtProt; NX_P02647; -.
DR OpenTargets; ENSG00000118137; -.
DR Orphanet; 93560; AApoAI amyloidosis.
DR Orphanet; 425; Apolipoprotein A-I deficiency.
DR PharmGKB; PA49; -.
DR VEuPathDB; HostDB:ENSG00000118137; -.
DR eggNOG; ENOG502S1XQ; Eukaryota.
DR GeneTree; ENSGT00950000182929; -.
DR HOGENOM; CLU_058447_1_0_1; -.
DR InParanoid; P02647; -.
DR OMA; KEVREMW; -.
DR OrthoDB; 1553412at2759; -.
DR PhylomeDB; P02647; -.
DR TreeFam; TF334458; -.
DR PathwayCommons; P02647; -.
DR Reactome; R-HSA-114608; Platelet degranulation.
DR Reactome; R-HSA-1369062; ABC transporters in lipid homeostasis.
DR Reactome; R-HSA-1989781; PPARA activates gene expression.
DR Reactome; R-HSA-2168880; Scavenging of heme from plasma.
DR Reactome; R-HSA-3000471; Scavenging by Class B Receptors.
DR Reactome; R-HSA-3000480; Scavenging by Class A Receptors.
DR Reactome; R-HSA-381426; Regulation of Insulin-like Growth Factor (IGF) transport and uptake by Insulin-like Growth Factor Binding Proteins (IGFBPs).
DR Reactome; R-HSA-5682113; Defective ABCA1 causes TGD.
DR Reactome; R-HSA-8957275; Post-translational protein phosphorylation.
DR Reactome; R-HSA-8963888; Chylomicron assembly.
DR Reactome; R-HSA-8963896; HDL assembly.
DR Reactome; R-HSA-8963901; Chylomicron remodeling.
DR Reactome; R-HSA-8964011; HDL clearance.
DR Reactome; R-HSA-8964058; HDL remodeling.
DR Reactome; R-HSA-9707616; Heme signaling.
DR Reactome; R-HSA-975634; Retinoid metabolism and transport.
DR Reactome; R-HSA-977225; Amyloid fiber formation.
DR SignaLink; P02647; -.
DR SIGNOR; P02647; -.
DR BioGRID-ORCS; 335; 12 hits in 1071 CRISPR screens.
DR ChiTaRS; APOA1; human.
DR EvolutionaryTrace; P02647; -.
DR GeneWiki; Apolipoprotein_A1; -.
DR GenomeRNAi; 335; -.
DR Pharos; P02647; Tbio.
DR PRO; PR:P02647; -.
DR Proteomes; UP000005640; Chromosome 11.
DR RNAct; P02647; protein.
DR Bgee; ENSG00000118137; Expressed in jejunal mucosa and 108 other tissues.
DR ExpressionAtlas; P02647; baseline and differential.
DR Genevisible; P02647; HS.
DR GO; GO:0072562; C:blood microparticle; HDA:UniProtKB.
DR GO; GO:0042627; C:chylomicron; IBA:GO_Central.
DR GO; GO:0062023; C:collagen-containing extracellular matrix; HDA:BHF-UCL.
DR GO; GO:0031410; C:cytoplasmic vesicle; IDA:BHF-UCL.
DR GO; GO:0005829; C:cytosol; TAS:Reactome.
DR GO; GO:0005769; C:early endosome; TAS:Reactome.
DR GO; GO:0030139; C:endocytic vesicle; IDA:BHF-UCL.
DR GO; GO:0071682; C:endocytic vesicle lumen; TAS:Reactome.
DR GO; GO:0005788; C:endoplasmic reticulum lumen; TAS:Reactome.
DR GO; GO:0070062; C:extracellular exosome; HDA:UniProtKB.
DR GO; GO:0005576; C:extracellular region; HDA:BHF-UCL.
DR GO; GO:0005615; C:extracellular space; IDA:MGI.
DR GO; GO:1903561; C:extracellular vesicle; HDA:UniProtKB.
DR GO; GO:0034364; C:high-density lipoprotein particle; IDA:BHF-UCL.
DR GO; GO:0005886; C:plasma membrane; TAS:Reactome.
DR GO; GO:0034774; C:secretory granule lumen; TAS:Reactome.
DR GO; GO:0034366; C:spherical high-density lipoprotein particle; IDA:BHF-UCL.
DR GO; GO:0034361; C:very-low-density lipoprotein particle; IDA:BHF-UCL.
DR GO; GO:0001540; F:amyloid-beta binding; IDA:BHF-UCL.
DR GO; GO:0034191; F:apolipoprotein A-I receptor binding; IPI:BHF-UCL.
DR GO; GO:0034190; F:apolipoprotein receptor binding; IPI:BHF-UCL.
DR GO; GO:0045499; F:chemorepellent activity; IDA:UniProtKB.
DR GO; GO:0015485; F:cholesterol binding; IDA:BHF-UCL.
DR GO; GO:0120020; F:cholesterol transfer activity; IMP:BHF-UCL.
DR GO; GO:0019899; F:enzyme binding; IPI:BHF-UCL.
DR GO; GO:0031072; F:heat shock protein binding; IPI:CAFA.
DR GO; GO:0008035; F:high-density lipoprotein particle binding; IEA:Ensembl.
DR GO; GO:0070653; F:high-density lipoprotein particle receptor binding; IPI:BHF-UCL.
DR GO; GO:0042802; F:identical protein binding; IPI:IntAct.
DR GO; GO:0031210; F:phosphatidylcholine binding; IBA:GO_Central.
DR GO; GO:0060228; F:phosphatidylcholine-sterol O-acyltransferase activator activity; IDA:BHF-UCL.
DR GO; GO:0005543; F:phospholipid binding; IDA:BHF-UCL.
DR GO; GO:0042803; F:protein homodimerization activity; ISS:UniProtKB.
DR GO; GO:0005102; F:signaling receptor binding; IPI:ARUK-UCL.
DR GO; GO:0030325; P:adrenal gland development; IEA:Ensembl.
DR GO; GO:0043534; P:blood vessel endothelial cell migration; IEA:Ensembl.
DR GO; GO:0006695; P:cholesterol biosynthetic process; IBA:GO_Central.
DR GO; GO:0033344; P:cholesterol efflux; IDA:BHF-UCL.
DR GO; GO:0042632; P:cholesterol homeostasis; IDA:BHF-UCL.
DR GO; GO:0070508; P:cholesterol import; IMP:BHF-UCL.
DR GO; GO:0008203; P:cholesterol metabolic process; IMP:BHF-UCL.
DR GO; GO:0030301; P:cholesterol transport; IDA:MGI.
DR GO; GO:0001935; P:endothelial cell proliferation; IEA:Ensembl.
DR GO; GO:0007186; P:G protein-coupled receptor signaling pathway; IDA:BHF-UCL.
DR GO; GO:0008211; P:glucocorticoid metabolic process; IEA:Ensembl.
DR GO; GO:0034380; P:high-density lipoprotein particle assembly; IDA:BHF-UCL.
DR GO; GO:0034384; P:high-density lipoprotein particle clearance; IC:BHF-UCL.
DR GO; GO:0034375; P:high-density lipoprotein particle remodeling; IDA:BHF-UCL.
DR GO; GO:0007229; P:integrin-mediated signaling pathway; IDA:UniProtKB.
DR GO; GO:0019915; P:lipid storage; IEA:Ensembl.
DR GO; GO:0042158; P:lipoprotein biosynthetic process; IEA:Ensembl.
DR GO; GO:0042157; P:lipoprotein metabolic process; IBA:GO_Central.
DR GO; GO:0050919; P:negative chemotaxis; IDA:UniProtKB.
DR GO; GO:0060354; P:negative regulation of cell adhesion molecule production; IDA:BHF-UCL.
DR GO; GO:0002719; P:negative regulation of cytokine production involved in immune response; IDA:BHF-UCL.
DR GO; GO:0034115; P:negative regulation of heterotypic cell-cell adhesion; IDA:BHF-UCL.
DR GO; GO:0051346; P:negative regulation of hydrolase activity; IEA:Ensembl.
DR GO; GO:0050728; P:negative regulation of inflammatory response; IDA:BHF-UCL.
DR GO; GO:0032691; P:negative regulation of interleukin-1 beta production; IDA:BHF-UCL.
DR GO; GO:0060761; P:negative regulation of response to cytokine stimulus; IDA:BHF-UCL.
DR GO; GO:0010804; P:negative regulation of tumor necrosis factor-mediated signaling pathway; IDA:BHF-UCL.
DR GO; GO:0010903; P:negative regulation of very-low-density lipoprotein particle remodeling; IDA:BHF-UCL.
DR GO; GO:0018206; P:peptidyl-methionine modification; IDA:UniProtKB.
DR GO; GO:0006656; P:phosphatidylcholine biosynthetic process; IDA:BHF-UCL.
DR GO; GO:0046470; P:phosphatidylcholine metabolic process; IBA:GO_Central.
DR GO; GO:0033700; P:phospholipid efflux; IDA:BHF-UCL.
DR GO; GO:0055091; P:phospholipid homeostasis; IDA:BHF-UCL.
DR GO; GO:0010875; P:positive regulation of cholesterol efflux; IDA:UniProtKB.
DR GO; GO:0010873; P:positive regulation of cholesterol esterification; IBA:GO_Central.
DR GO; GO:0090205; P:positive regulation of cholesterol metabolic process; IDA:BHF-UCL.
DR GO; GO:1905920; P:positive regulation of CoA-transferase activity; IDA:BHF-UCL.
DR GO; GO:0045723; P:positive regulation of fatty acid biosynthetic process; IBA:GO_Central.
DR GO; GO:0051345; P:positive regulation of hydrolase activity; IDA:BHF-UCL.
DR GO; GO:0046889; P:positive regulation of lipid biosynthetic process; IBA:GO_Central.
DR GO; GO:0051006; P:positive regulation of lipoprotein lipase activity; IBA:GO_Central.
DR GO; GO:0050766; P:positive regulation of phagocytosis; IDA:UniProtKB.
DR GO; GO:1902995; P:positive regulation of phospholipid efflux; IDA:UniProtKB.
DR GO; GO:0035025; P:positive regulation of Rho protein signal transduction; IDA:UniProtKB.
DR GO; GO:0051496; P:positive regulation of stress fiber assembly; IDA:UniProtKB.
DR GO; GO:1900026; P:positive regulation of substrate adhesion-dependent cell spreading; IDA:UniProtKB.
DR GO; GO:0010898; P:positive regulation of triglyceride catabolic process; IBA:GO_Central.
DR GO; GO:0018158; P:protein oxidation; IDA:UniProtKB.
DR GO; GO:0050821; P:protein stabilization; IDA:UniProtKB.
DR GO; GO:0032489; P:regulation of Cdc42 protein signal transduction; IDA:BHF-UCL.
DR GO; GO:0030300; P:regulation of intestinal cholesterol absorption; IBA:GO_Central.
DR GO; GO:0001932; P:regulation of protein phosphorylation; IEA:Ensembl.
DR GO; GO:0043691; P:reverse cholesterol transport; IMP:BHF-UCL.
DR GO; GO:0070328; P:triglyceride homeostasis; IDA:BHF-UCL.
DR GO; GO:0034372; P:very-low-density lipoprotein particle remodeling; IBA:GO_Central.
DR GO; GO:0051180; P:vitamin transport; IMP:AgBase.
DR InterPro; IPR000074; ApoA_E.
DR Pfam; PF01442; Apolipoprotein; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Amyloid; Amyloidosis; Atherosclerosis;
KW Cholesterol metabolism; Direct protein sequencing; Disease variant;
KW Glycation; Glycoprotein; HDL; Lipid metabolism; Lipid transport;
KW Lipoprotein; Neuropathy; Oxidation; Palmitate; Phosphoprotein;
KW Reference proteome; Repeat; Secreted; Signal; Steroid metabolism;
KW Sterol metabolism; Transport.
FT SIGNAL 1..18
FT /evidence="ECO:0000269|PubMed:6328445,
FT ECO:0000269|PubMed:6409108"
FT CHAIN 19..267
FT /note="Proapolipoprotein A-I"
FT /id="PRO_0000425323"
FT CHAIN 25..267
FT /note="Apolipoprotein A-I"
FT /id="PRO_0000001939"
FT CHAIN 25..266
FT /note="Truncated apolipoprotein A-I"
FT /id="PRO_0000001940"
FT REPEAT 68..89
FT /note="1"
FT REPEAT 90..111
FT /note="2"
FT REPEAT 112..122
FT /note="3; half-length"
FT REPEAT 123..144
FT /note="4"
FT REPEAT 145..166
FT /note="5"
FT REPEAT 167..188
FT /note="6"
FT REPEAT 189..210
FT /note="7"
FT REPEAT 211..232
FT /note="8"
FT REPEAT 233..243
FT /note="9; half-length"
FT REPEAT 244..267
FT /note="10"
FT REGION 68..267
FT /note="10 X approximate tandem repeats"
FT MOD_RES 110
FT /note="Methionine sulfoxide"
FT /evidence="ECO:0000269|PubMed:12576517"
FT MOD_RES 136
FT /note="Methionine sulfoxide"
FT /evidence="ECO:0000269|PubMed:12576517"
FT CARBOHYD 263
FT /note="N-linked (Glc) (glycation) lysine"
FT /evidence="ECO:0000269|PubMed:8261628"
FT VARIANT 23..267
FT /note="Missing (in FHA2; no protein expression)"
FT /evidence="ECO:0000269|PubMed:8282791"
FT /id="VAR_083307"
FT VARIANT 27
FT /note="P -> H (in Munster-3C; dbSNP:rs121912720)"
FT /id="VAR_000605"
FT VARIANT 27
FT /note="P -> R (in dbSNP:rs121912720)"
FT /evidence="ECO:0000269|PubMed:2512329"
FT /id="VAR_000606"
FT VARIANT 28
FT /note="P -> R (in Munster-3B; dbSNP:rs121912721)"
FT /evidence="ECO:0000269|PubMed:2512329"
FT /id="VAR_000607"
FT VARIANT 34
FT /note="R -> L (in Baltimore; dbSNP:rs28929476)"
FT /evidence="ECO:0000269|PubMed:2108924"
FT /id="VAR_000608"
FT VARIANT 50
FT /note="G -> R (in AMYL8; also found in a family with
FT amyloid polyneuropathy-nephropathy Iowa; dbSNP:rs28931574)"
FT /evidence="ECO:0000269|PubMed:12050338,
FT ECO:0000269|PubMed:2123470, ECO:0000269|PubMed:3142462,
FT ECO:0000269|PubMed:8208902"
FT /id="VAR_000609"
FT VARIANT 56..267
FT /note="Missing (in HDL deficiency; with periorbital
FT xanthelasmas; decreased protein abundance)"
FT /evidence="ECO:0000269|PubMed:7981179"
FT /id="VAR_083308"
FT VARIANT 61
FT /note="A -> T (in dbSNP:rs12718465)"
FT /evidence="ECO:0000269|PubMed:15108119,
FT ECO:0000269|PubMed:1901417"
FT /id="VAR_025445"
FT VARIANT 84
FT /note="L -> R (in AMYL8; dbSNP:rs121912724)"
FT /evidence="ECO:0000269|PubMed:1502149"
FT /id="VAR_000610"
FT VARIANT 92
FT /note="T -> I (confirmed at protein level;
FT dbSNP:rs766422306)"
FT /evidence="ECO:0000269|PubMed:12966036,
FT ECO:0000269|PubMed:22028381"
FT /id="VAR_017017"
FT VARIANT 108..267
FT /note="Missing (in FHA2; missing protein expression)"
FT /evidence="ECO:0000269|PubMed:1901417"
FT /id="VAR_083309"
FT VARIANT 113
FT /note="D -> E (in dbSNP:rs150243849)"
FT /evidence="ECO:0000269|PubMed:2111322"
FT /id="VAR_000611"
FT VARIANT 119
FT /note="A -> D (in Hita)"
FT /id="VAR_000612"
FT VARIANT 126
FT /note="D -> H (in dbSNP:rs5077)"
FT /id="VAR_016189"
FT VARIANT 127
FT /note="D -> N (in Munster-3A; dbSNP:rs921646982)"
FT /id="VAR_000613"
FT VARIANT 131
FT /note="K -> M (in dbSNP:rs4882)"
FT /evidence="ECO:0000269|PubMed:2111322"
FT /id="VAR_000615"
FT VARIANT 131
FT /note="Missing (in Marburg/Munster-2)"
FT /id="VAR_000614"
FT VARIANT 132
FT /note="W -> R (in Tsushima)"
FT /id="VAR_000616"
FT VARIANT 134
FT /note="E -> K (in Fukuoka)"
FT /evidence="ECO:0000269|PubMed:2107878"
FT /id="VAR_000617"
FT VARIANT 160
FT /note="E -> K (in Norway; dbSNP:rs121912718)"
FT /evidence="ECO:0000269|PubMed:6432779"
FT /id="VAR_000618"
FT VARIANT 163
FT /note="E -> G (in dbSNP:rs758509542)"
FT /evidence="ECO:0000269|PubMed:2111322"
FT /id="VAR_000619"
FT VARIANT 167
FT /note="P -> R (in Giessen; dbSNP:rs121912719)"
FT /evidence="ECO:0000269|PubMed:6489332"
FT /id="VAR_000620"
FT VARIANT 168
FT /note="L -> R (in Zaragoza)"
FT /evidence="ECO:0000269|Ref.62"
FT /id="VAR_000621"
FT VARIANT 171
FT /note="E -> V (in dbSNP:rs1015066427)"
FT /evidence="ECO:0000269|PubMed:2111322"
FT /id="VAR_000622"
FT VARIANT 173
FT /note="R -> P (in AMYL8; unknown pathological
FT significance)"
FT /evidence="ECO:0000269|PubMed:10198255"
FT /id="VAR_083310"
FT VARIANT 173
FT /note="R -> S (in Boston; no evidence of association with
FT premature coronary heart disease; associated with decreased
FT levels of HDL cholesterol; associated with decreased serum
FT cellular cholesterol efflux; associated with decreased
FT lecithin-cholesterol acyltransferase (LCAT) activity)"
FT /evidence="ECO:0000269|PubMed:26073399"
FT /id="VAR_074073"
FT VARIANT 180
FT /note="V -> E (in Oita; 60% of normal apoA-I and normal HDL
FT cholesterol levels; rapidly cleared from plasma;
FT dbSNP:rs121912727)"
FT /evidence="ECO:0000269|PubMed:9514407"
FT /id="VAR_021362"
FT VARIANT 184
FT /note="R -> P (in dbSNP:rs5078)"
FT /id="VAR_014609"
FT VARIANT 189
FT /note="P -> R (in dbSNP:rs121912722)"
FT /evidence="ECO:0000269|PubMed:2512329"
FT /id="VAR_000623"
FT VARIANT 197
FT /note="R -> C (in Milano; no evidence of association with
FT premature vascular disease; associated with decreased HDL
FT levels and moderate increase in triglycerides; allows the
FT formation of disulfide-linked homodimers via the introduced
FT cysteine; assembles properly in HDL; alters protein
FT structure; has no tendency to form fibrils and aggregates;
FT dbSNP:rs28931573)"
FT /evidence="ECO:0000269|PubMed:24755625,
FT ECO:0000269|PubMed:6401735"
FT /id="VAR_000624"
FT VARIANT 198
FT /note="L -> S (in AMYL8; plasma level of HDL and apoA-I
FT protein were significantly lower in the patient)"
FT /evidence="ECO:0000269|PubMed:10487826"
FT /id="VAR_083311"
FT VARIANT 199
FT /note="A -> P (in AMYL8; unknown pathological
FT significance)"
FT /evidence="ECO:0000269|PubMed:12050338"
FT /id="VAR_083312"
FT VARIANT 222
FT /note="E -> K (in Munster-4; dbSNP:rs121912717)"
FT /evidence="ECO:0000269|PubMed:2111322"
FT /id="VAR_000625"
FT CONFLICT 32
FT /note="W -> P (in Ref. 25; AA sequence)"
FT /evidence="ECO:0000305"
FT HELIX 33..42
FT /evidence="ECO:0007829|PDB:3R2P"
FT HELIX 45..59
FT /evidence="ECO:0007829|PDB:3R2P"
FT HELIX 61..65
FT /evidence="ECO:0007829|PDB:3R2P"
FT HELIX 82..110
FT /evidence="ECO:0007829|PDB:7KJR"
FT HELIX 113..119
FT /evidence="ECO:0007829|PDB:6PTW"
FT TURN 159..164
FT /evidence="ECO:0007829|PDB:3R2P"
FT HELIX 166..203
FT /evidence="ECO:0007829|PDB:3R2P"
FT TURN 229..232
FT /evidence="ECO:0007829|PDB:2MSC"
FT HELIX 233..260
FT /evidence="ECO:0007829|PDB:2MSC"
SQ SEQUENCE 267 AA; 30778 MW; 1A28B8366E620310 CRC64;
MKAAVLTLAV LFLTGSQARH FWQQDEPPQS PWDRVKDLAT VYVDVLKDSG RDYVSQFEGS
ALGKQLNLKL LDNWDSVTST FSKLREQLGP VTQEFWDNLE KETEGLRQEM SKDLEEVKAK
VQPYLDDFQK KWQEEMELYR QKVEPLRAEL QEGARQKLHE LQEKLSPLGE EMRDRARAHV
DALRTHLAPY SDELRQRLAA RLEALKENGG ARLAEYHAKA TEHLSTLSEK AKPALEDLRQ
GLLPVLESFK VSFLSALEEY TKKLNTQ
